Structure of PDB 3umm Chain A

Receptor sequence

>3ummA (length=1285) Species: 90371 (Salmonella enterica subsp. enterica serovar Typhimurium)

GLVPRGSHMMEILRGSPALSAFRINKLLARFQAANLQVHNIYAEYVHFAD
LNAPLNDSEQAQLTRLLQYGPALSSHTPAGKLLLVTPRPGTISPWSSKAT
DIAHNCGLQQVDRLERGVAYYIEASTLTAEQWRQVAAELHDRMMETVFSS
LTDAEKLFIHHQPAPVSSVDLLGEGRQALIDANLRLGLALAEDEIDYLQE
AFTKLGRNPNDIELYMFAQANSEHCRHKIFNADWIIDGKPQPKSLFKMIK
NTFETTPDYVLSAYKDNAAVMEGSAVGRYFADHNTGRYDFHQEPAHILMK
VETHNHPTAISPWPGAATGSGGEIRDEGATGRGAKPKAGLVGFSVSNLRI
PGFEQPWEEDFGKPERIVTALDIMTEGPLGGAAFNNEFGRPALTGYFRTY
EEKVNSHNGEELRGYHKPIMLAGGIGNIRADHVQKGEIVVGAKLIVLGGP
AMNIGDFASVQRDNPEMERRCQEVIDRCWQLGDANPILFIHDVGAGGLSN
AMPELVSDGGRGGKFELRDILSDEPGMSPLEIWCNESQERYVLAVAADQL
PLFDELCKRERAPYAVIGDATEEQHLSLHDNHFDNQPIDLPLDVLLGKTP
KMTRDVQTLKAKGDALNRADITIADAVKRVLHLPTVAEKTFLVTIGDRTV
TGMVARDQMVGPWQVPVADCAVTTASLDSYYGEAMSIGERAPVALLDFAA
SARLAVGEALTNIAATQIGDIKRIKLSANWMAAAGHPGEDAGLYDAVKAV
GEELCPQLGLTIPVGKDSMSMKTRWQEGNEQREMTSPLSLVISAFARVED
VRHTLTPQLSTEDNALLLIDLGKGHNALGATALAQVYRQLGDKPADVRDV
AQLKGFYDAMQALVAARKLLAWHDRSDGGLLVTLAEMAFAGHCGVQVDIA
ALGDDHLAALFNEELGGVIQVRAEDRDAVEALLAQYGLADCVHYLGQALA
GDRFVITANDQTVFSESRTTLRVWWAETTWQMQRLRDNPQCADQEHEAKA
NDTDPGLNVKLSFDINEDIAAPYIATGARPKVAVLREQGVNSHVEMAAAF
HRAGFDAIDVHMSDLLGGRIGLGNFHALVACGGFSYGDVLGAGEGWAKSI
LFNHRVRDEFETFFHRPQTLALGVCNGCQMMSNLRELIPGSELWPRFVRN
HSDRFEARFSLVEVTQSPSLLLQGMVGSQMPIAVSHGEGRVEVRDDAHLA
ALESKGLVALRYVDNFGKVTETYPANPNGSPNGITAVTTENGRVTIMMPH
PERVFRTVANSWHPENWGEDSPWMRIFRNARKQLG

3D structure

• PDB: 3umm Formylglycinamide ribonucleotide amidotransferase from Salmonella typhimurium: role of ATP complexation and the glutaminase domain in catalytic coupling
• Chain: A
• Resolution: 3.2 Å

Enzymatic activity

• Enzyme Commision number: 6.3.5.3: phosphoribosylformylglycinamidine synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ANP	A	H219 F222 D258 N259 K292 E294 D318 D502 V774 G775 K776	H227 F230 D266 N267 K300 E302 D326 D492 V764 G765 K766
BS02	ADP	A	T386 G387 Y388 L652 Q668 A678 N722	T394 G395 Y396 L642 Q658 A668 N712
BS03	MG	A	D679 N722 D884	D669 N712 D874

Gene Ontology

Molecular Function

• GO:0004642 phosphoribosylformylglycinamidine synthase activity
• GO:0005524 ATP binding
• GO:0016874 ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006164 purine nucleotide biosynthetic process
• GO:0006189 'de novo' IMP biosynthetic process
• GO:0006541 glutamine metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3umm, PDBe:3umm, PDBj:3umm
• PDBsum: 3umm
• PubMed: 22683785
• UniProt: P74881|PUR4_SALTY Phosphoribosylformylglycinamidine synthase (Gene Name=purL)